Analytical Data
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Gene name
FDXR
- Application
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Alternative Names
FDXR；ADXR；NADPH:adrenodoxin oxidoreductase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22570
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Expression Region
33-451aa
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AA Sequence
STQEKTPQICVVGSGPAGFYTAQHLLKQHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH
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Molecular Weight
58.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
FDXR (ferredoxin reductase) is a crucial enzyme involved in the electron transport chain, facilitating the transfer of electrons from NADPH to ferredoxin, which is vital for various biochemical processes, including photosynthesis and nitrogen fixation in plants and microorganisms. The study of FDXR has gained attention due to its role in cellular metabolism and potential implications in biotechnology and medicine. Research has highlighted its importance in the biosynthesis of essential metabolites and in maintaining redox balance within cells. Additionally, altered FDXR activity has been associated with various diseases, including cancer and metabolic disorders, making it a potential target for therapeutic interventions. Recent advances in recombinant protein technology have enabled the production and characterization of FDXR, allowing researchers to investigate its structure-function relationships and enzymatic mechanisms in depth. Understanding the biochemical properties of FDXR not only enhances our knowledge of fundamental biological processes but also opens avenues for engineering this enzyme for applications in sustainable agriculture and the development of novel therapeutics. The ongoing exploration of FDXR could lead to significant advancements in both basic and applied sciences.
